...
首页> 外文期刊>Protein Science: A Publication of the Protein Society >A 2.08?? resolution structure of HLB5, a novel cellulase from the anaerobic gut bacterium Parabacteroides johnsonii DSM 18315 Parabacteroides johnsonii DSM 18315
【24h】

A 2.08?? resolution structure of HLB5, a novel cellulase from the anaerobic gut bacterium Parabacteroides johnsonii DSM 18315 Parabacteroides johnsonii DSM 18315

机译:一个2.08 ?? HLB5的分辨率结构,一种来自厌氧肠道细菌术的新型纤维素酶,Johnsonii dsm 18315临床johnsonii dsm 18315

获取原文
获取原文并翻译 | 示例
           

摘要

Abstract Cellulases play a significant role in the degradation of complex carbohydrates. In the human gut, anaerobic bacteria are essential to the well‐being of the host by producing these essential enzymes that convert plant polymers into simple sugars that can then be further metabolized by the host. Here, we report the 2.08?? resolution structure of HLB5, a chemically verified cellulase that was identified previously from an anaerobic gut bacterium and that has no structural cellulase homologues in PDB nor possesses any conserved region typical for glycosidases. We anticipate that the information presented here will facilitate the identification of additional cellulases for which no homologues have been identified to date and enhance our understanding how these novel cellulases bind and hydrolyze their substrates.
机译:摘要纤维素酶在复合碳水化合物的降解中起着重要作用。 在人体肠道中,通过产生将植物聚合物转化为宿主的简单糖,厌氧细菌对宿主的福祉至关重要。然后可以通过宿主进一步代谢。 在这里,我们报告2.08? HLB5的分辨率结构,一种先前从厌氧肠道细菌中鉴定的化学证明纤维素酶,并且在PDB中没有结构纤维素酶同源物,也没有具有典型的糖磷酸酶的任何保守区域。 我们预期此处提出的信息将促进鉴定额外的纤维素酶,其中没有鉴定出迄今为止的同源物,并增强这些新的纤维素酶如何结合和水解它们的基材。

著录项

相似文献

  • 外文文献
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号